ID   GSA_PICTO               Reviewed;         420 AA.
AC   Q6L2G9;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA {ECO:0000255|HAMAP-Rule:MF_00375};
DE            EC=5.4.3.8 {ECO:0000255|HAMAP-Rule:MF_00375};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT {ECO:0000255|HAMAP-Rule:MF_00375};
GN   Name=hemL {ECO:0000255|HAMAP-Rule:MF_00375}; OrderedLocusNames=PTO0248;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate;
CC         Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416;
CC         EC=5.4.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00375};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00375};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00375}.
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DR   EMBL; AE017261; AAT42833.1; -; Genomic_DNA.
DR   RefSeq; WP_011177049.1; NC_005877.1.
DR   AlphaFoldDB; Q6L2G9; -.
DR   SMR; Q6L2G9; -.
DR   STRING; 263820.PTO0248; -.
DR   EnsemblBacteria; AAT42833; AAT42833; PTO0248.
DR   GeneID; 2844133; -.
DR   KEGG; pto:PTO0248; -.
DR   PATRIC; fig|263820.9.peg.266; -.
DR   eggNOG; arCOG00918; Archaea.
DR   HOGENOM; CLU_016922_1_5_2; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 10264at2157; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000000438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR   InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00713; hemL; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..420
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000120487"
FT   MOD_RES         261
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   420 AA;  46628 MW;  069E07BF383C811F CRC64;
     MKGDDLFSEA LKLFPSGVNS PVRFYRPVPV MFERGRGSRI YDVNGKEYID YSLGFGPMIL
     GHADPDVASA IKRQADNGIL FGSITENEVR LGNIIKNHVK SIEKMRFTNS GTEATMHAIR
     LARGYTKRKY ILKMEGGFHG AHDYALIKSG SGTMTFGVPS SNGVPEEITK TVLVGKYNDE
     NSIESLFNEY GNDIAAVITE PILGNIGVIN PEPGFLEFLR EITNKYNSLL IFDEVITGFR
     FAFSGYQDII NIKPDITTMG KIIGGGAPIG LFGSSSEIMD LISPSGNVYE SGTFSGNPLS
     MAAGIAAMEK LQGMDYSRIN NYTADLVKSL YDIFNDKNID VNINHYGSMF QIFFNKNEVK
     TYDDAIKSDK DRFFKFFKKM LDHNVYLPPS QFETNFVSFA HGRDDLNKTI EAAKEAVSCI